Carbonization of a stable β-sheet-rich silk protein into a pseudographitic pyroprotein

Se Youn Cho, Young Soo Yun, Sungho Lee, Dawon Jang, Kyu-Young Park, Jae Kyung Kim, Byung Hoon Kim, Kisuk Kang, David L. Kaplan and Hyoung-Joon Jin ()
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Se Youn Cho: Inha University
Young Soo Yun: Inha University
Sungho Lee: Carbon Convergence Materials Research Center, Korea Institute of Science and Technology
Dawon Jang: Carbon Convergence Materials Research Center, Korea Institute of Science and Technology
Kyu-Young Park: Seoul National University
Jae Kyung Kim: Incheon National University
Byung Hoon Kim: Incheon National University
Kisuk Kang: Seoul National University
David L. Kaplan: Tufts University
Hyoung-Joon Jin: Inha University

Nature Communications, 2015, vol. 6, issue 1, 1-7

Abstract: Abstract Silk proteins are of great interest to the scientific community owing to their unique mechanical properties and interesting biological functionality. In addition, the silk proteins are not burned out following heating, rather they are transformed into a carbonaceous solid, pyroprotein; several studies have identified potential carbon precursors for state-of-the-art technologies. However, no mechanism for the carbonization of proteins has yet been reported. Here we examine the structural and chemical changes of silk proteins systematically at temperatures above the onset of thermal degradation. We find that the β-sheet structure is transformed into an sp2-hybridized carbon hexagonal structure by simple heating to 350 °C. The pseudographitic crystalline layers grew to form highly ordered graphitic structures following further heating to 2,800 °C. Our results provide a mechanism for the thermal transition of the protein and demonstrate a potential strategy for designing pyroproteins using a clean system with a catalyst-free aqueous wet process for in vivo applications.

Date: 2015
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DOI: 10.1038/ncomms8145

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